Max Crispin

19.2k total citations · 3 hit papers
157 papers, 9.1k citations indexed

About

Max Crispin is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Max Crispin has authored 157 papers receiving a total of 9.1k indexed citations (citations by other indexed papers that have themselves been cited), including 101 papers in Molecular Biology, 64 papers in Radiology, Nuclear Medicine and Imaging and 53 papers in Immunology. Recurrent topics in Max Crispin's work include Glycosylation and Glycoproteins Research (81 papers), Monoclonal and Polyclonal Antibodies Research (64 papers) and HIV Research and Treatment (50 papers). Max Crispin is often cited by papers focused on Glycosylation and Glycoproteins Research (81 papers), Monoclonal and Polyclonal Antibodies Research (64 papers) and HIV Research and Treatment (50 papers). Max Crispin collaborates with scholars based in United Kingdom, United States and Netherlands. Max Crispin's co-authors include Yasunori Watanabe, Joel D. Allen, David J. Harvey, Thomas A. Bowden, Raymond A. Dwek, Jason S. McLellan, Christopher N. Scanlan, Ian A. Wilson, Daniel Wrapp and Katie J. Doores and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Max Crispin

150 papers receiving 9.0k citations

Hit Papers

Site-specific glycan anal... 2019 2026 2021 2023 2020 2020 2019 250 500 750 1000

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Max Crispin 4.9k 3.0k 2.5k 2.3k 1.8k 157 9.1k
Robyn L. Stanfield 6.7k 1.4× 2.1k 0.7× 5.5k 2.2× 5.4k 2.4× 5.4k 3.1× 120 13.5k
Kenneth H. Roux 3.2k 0.7× 913 0.3× 2.7k 1.1× 1.9k 0.8× 2.0k 1.2× 152 9.2k
Ian M. Jones 3.3k 0.7× 1.7k 0.6× 1.7k 0.7× 844 0.4× 2.5k 1.4× 177 8.1k
Michael B. Zwick 3.4k 0.7× 2.0k 0.7× 3.3k 1.3× 3.2k 1.4× 5.5k 3.1× 77 8.2k
Erica Ollmann Saphire 2.5k 0.5× 5.0k 1.7× 2.1k 0.8× 1.8k 0.8× 2.0k 1.1× 152 8.9k
Jacob V. Maizel 9.7k 2.0× 2.3k 0.8× 1.5k 0.6× 1.0k 0.5× 1.3k 0.7× 171 15.4k
Jan Wilschut 5.5k 1.1× 3.3k 1.1× 2.6k 1.0× 457 0.2× 879 0.5× 232 12.5k
Louis E. Henderson 4.5k 0.9× 2.5k 0.8× 1.9k 0.8× 493 0.2× 4.4k 2.5× 94 8.9k
Stephen Oroszlan 4.5k 0.9× 3.4k 1.1× 2.9k 1.2× 1.0k 0.5× 4.9k 2.8× 197 11.2k
Timothy M. Block 4.4k 0.9× 1.9k 0.6× 2.4k 1.0× 479 0.2× 922 0.5× 232 12.6k

Countries citing papers authored by Max Crispin

Since Specialization
Citations

This map shows the geographic impact of Max Crispin's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Max Crispin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Max Crispin more than expected).

Fields of papers citing papers by Max Crispin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Max Crispin. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Max Crispin. The network helps show where Max Crispin may publish in the future.

Co-authorship network of co-authors of Max Crispin

This figure shows the co-authorship network connecting the top 25 collaborators of Max Crispin. A scholar is included among the top collaborators of Max Crispin based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Max Crispin. Max Crispin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Kumar, Sanjeev, Iván del Moral-Sánchez, Maddy L. Newby, et al.. (2025). The Design and Immunogenicity of an HIV-1 Clade C Pediatric Envelope Glycoprotein Stabilized by Multiple Platforms. Vaccines. 13(2). 110–110. 1 indexed citations
2.
Newby, Maddy L., Joel D. Allen, Giorgia Chiodin, et al.. (2025). The origin, diagnosis, and prognosis of oligomannose-type diffuse large B-cell lymphoma. Blood. 146(23). 2808–2820.
3.
Kim, Young Chan, Yasunori Watanabe, Xiyong Song, et al.. (2024). Immunogenic recombinant Mayaro virus-like particles present natively assembled glycoprotein. npj Vaccines. 9(1). 243–243. 3 indexed citations
4.
Perrett, Hailee R., Philip J. M. Brouwer, Jonathan Hurtado, et al.. (2023). Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies. Cell Reports. 42(5). 112524–112524. 14 indexed citations
5.
Ringe, Rajesh P., Philippe Colin, Gabriel Ozorowski, et al.. (2023). Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization. PLoS Pathogens. 19(10). e1011601–e1011601. 5 indexed citations
6.
Moral-Sánchez, Iván del, Rebecca A. Russell, Edith E. Schermer, et al.. (2022). High thermostability improves neutralizing antibody responses induced by native-like HIV-1 envelope trimers. npj Vaccines. 7(1). 27–27. 12 indexed citations
7.
Khan, Abdullah O., Jasmeet S. Reyat, Joshua H. Bourne, et al.. (2022). Preferential uptake of SARS-CoV-2 by pericytes potentiates vascular damage and permeability in an organoid model of the microvasculature. Cardiovascular Research. 118(15). 3085–3096. 20 indexed citations
8.
Jinks, Elizabeth, Tracey A. Haigh, Baksho Kaul, et al.. (2022). Mutations in SARS-CoV-2 spike protein impair epitope-specific CD4+ T cell recognition. Nature Immunology. 23(12). 1726–1734. 19 indexed citations
9.
Samsudin, Firdaus, Jan K. Marzinek, Conrado Pedebos, et al.. (2022). Uncovering cryptic pockets in the SARS-CoV-2 spike glycoprotein. Structure. 30(8). 1062–1074.e4. 25 indexed citations
10.
Allen, Joel D., et al.. (2021). Suppression of O-Linked Glycosylation of the SARS-CoV-2 Spike by Quaternary Structural Restraints. Analytical Chemistry. 93(43). 14392–14400. 13 indexed citations
11.
Lee, Chang‐Chun D., Yasunori Watanabe, Nicholas C. Wu, et al.. (2021). A cross-neutralizing antibody between HIV-1 and influenza virus. PLoS Pathogens. 17(3). e1009407–e1009407. 23 indexed citations
12.
Hangartner, Lars, Eva G. Rakasz, Rebecca Nedellec, et al.. (2021). Effector function does not contribute to protection from virus challenge by a highly potent HIV broadly neutralizing antibody in nonhuman primates. Science Translational Medicine. 13(585). 26 indexed citations
13.
Yu, Xiaojie, Sonya James, James H. Felce, et al.. (2021). TNF receptor agonists induce distinct receptor clusters to mediate differential agonistic activity. Communications Biology. 4(1). 772–772. 35 indexed citations
14.
Watanabe, Yasunori, Zachary T. Berndsen, Jayna Raghwani, et al.. (2020). Vulnerabilities in coronavirus glycan shields despite extensive glycosylation. Nature Communications. 11(1). 2688–2688. 240 indexed citations
15.
Watanabe, Yasunori, Joel D. Allen, Daniel Wrapp, Jason S. McLellan, & Max Crispin. (2020). Site-specific glycan analysis of the SARS-CoV-2 spike. Science. 369(6501). 330–333. 1041 indexed citations breakdown →
16.
Tokatlian, Talar, Benjamin J. Read, Christopher A. Jones, et al.. (2018). Innate immune recognition of glycans targets HIV nanoparticle immunogens to germinal centers. Science. 363(6427). 649–654. 212 indexed citations
17.
Järnum, Sofia, Anna Runström, Robert Bockermann, et al.. (2017). Enzymatic Inactivation of Endogenous IgG by IdeS Enhances Therapeutic Antibody Efficacy. Molecular Cancer Therapeutics. 16(9). 1887–1897. 9 indexed citations
18.
Hofmann, Johanna, et al.. (2017). Identification of Lewis and Blood Group Carbohydrate Epitopes by Ion Mobility-Tandem-Mass Spectrometry Fingerprinting. Analytical Chemistry. 89(4). 2318–2325. 60 indexed citations
19.
Dalziel, Martin, Max Crispin, Christopher N. Scanlan, Nicole Zitzmann, & Raymond A. Dwek. (2014). Emerging Principles for the Therapeutic Exploitation of Glycosylation. Science. 343(6166). 1235681–1235681. 369 indexed citations
20.
Doores, Katie J., Camille Bonomelli, David J. Harvey, et al.. (2010). Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proceedings of the National Academy of Sciences. 107(31). 13800–13805. 263 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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